ADAMTS3
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Official Full Name
ADAM metallopeptidase with thrombospondin type 1 motif, 3 -
Overview
This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. Members of the family share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. The protein encoded by this gene is the major procollagen II N-propeptidase. A deficiency of this protein may be responsible for dermatosparaxis, a genetic defect of connective tissues. [provided by RefSeq, Jul 2008] -
Synonyms
ADAMTS3;ADAM metallopeptidase with thrombospondin type 1 motif, 3;ADAMTS-4;A disintegrin and metalloproteinase with thrombospondin motifs 3;ADAM-TS3;ADAMTS-3;PC II-NP;ADAM-TS 3;zinc metalloendopeptidase;procollagen II N-proteinase;procollagen II amino propeptide-processing enzyme;a disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 3
Recombinant Proteins
- Human
- Zebrafish
- Mouse
- E.coli
- E.Coli/Yeast
- Wheat Germ
- Mammalian Cells
- HEK293
- Human Cells
- His
- GST
- Non
- Myc&DDK
- Flag
- His&Fc&Avi
Involved Pathway
ADAMTS3 involved in several pathways and played different roles in them. We selected most pathways ADAMTS3 participated on our site, such as Collagen biosynthesis and modifying enzymes,Collagen formation,Extracellular matrix organization, which may be useful for your reference. Also, other proteins which involved in the same pathway with ADAMTS3 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|---|
| Extracellular matrix organization | ELANE,ICAM4,PRP,MMP20,TLDC2,LEPREL1,JAM2B,PCOLCE,COMP,EFEMP2 |
| O-linked glycosylation | GCNT3,ADAMTS13,ADAMTSL3,B3GNT8,ADAMTS4,GALNT13,SSPO,ADAMTS15,SPON1,MUC1 |
| Post-translational protein modification | TMED2,NSMCE1,SEC22C,ZNF408,DOHH,PPP6R3,MUC4,PROZ,GNE,CNIH |
| Metabolism of proteins | EXOC1,KLHDC3,NAT8,FBXW2,IGFBP5B,CBX8,MAN1A2,DPH5,GPR120,IGFBP5 |
| Collagen formation | ADAMTS2,LOXL2,SERPINH1,COL16A1,MMP13,COL28A1A,PCOLCEA,COL9A3,COL9A1B,COL10A1 |
| O-glycosylation of TSR domain-containing proteins | SPON1A,ADAMTSL4,ADAMTS5,SPON1,ADAMTS8,SPON1B,ADAMTS15,ADAMTS10,ADAMTS18,THSD7A |
| Collagen biosynthesis and modifying enzymes | COL4A4,COL17A1A,EMID2,BMP1A,PCOLCEB,COL8A1A,COL9A1B,COL4A3,COL10A1A,COL9A1 |
Protein Function
ADAMTS3 has several biochemical functions, for example, endopeptidase activity,heparin binding,metalloendopeptidase activity. Some of the functions are cooperated with other proteins, some of the functions could acted by ADAMTS3 itself. We selected most functions ADAMTS3 had, and list some proteins which have the same functions with ADAMTS3. You can find most of the proteins on our site.
| Function | Related Protein |
|---|---|
| protein binding | PIK3CB,COX5B,SELPLG,FOXP4,YEATS4,GLI1,ATP10A,POLR1D,SIX1,ZNF750 |
| zinc ion binding | BRF1,MARCH3,HLTF,ZDHHC14,MKRN3,PHC3,CUL9,ZDHHC1,CALB1,TRIM74 |
| endopeptidase activity | PSMA3,FURIN,FAP,MMP12,REN2,SENP1,PSMA2,HTRA4,RHBDD1,PSEN2 |
| heparin binding | FGF14,CXCL10,SOST,THBS2,UBE4A,APLP2,SERPINE2,REG4,FGF12,SLIT1A |
| metalloendopeptidase activity | XRCC6BP1,KEL,FAP,ADAMDEC1,NRD1B,MMP30,NLN,MMP11,ADAM23,MEP1B |
Interacting Protein
ADAMTS3 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with ADAMTS3 here. Most of them are supplied by our site. Hope this information will be useful for your research of ADAMTS3.
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References
- Pyun, JA; Kim, S; et al. Genome-wide association studies and epistasis analyses of candidate genes related to age at menarche and age at natural menopause in a Korean population. MENOPAUSE-THE JOURNAL OF THE NORTH AMERICAN MENOPAUSE SOCIETY 21:522-529(2014).
- Chaemsaithong, P; Madan, I; et al. Characterization of the myometrial transcriptome in women with an arrest of dilatation during labor. JOURNAL OF PERINATAL MEDICINE 41:665-681(2013).
